Crystal structure of isoamyl acetate-hydrolyzing esterase from Saccharomyces cerevisiae reveals a novel active site architecture and the basis of substrate specificity

Proteins: Structure, Function and Bioinformatics

Volumn 79, Issue 2, 2011, Pages 662-668

  Ma, Jinming ^a,b   Lu, Qianda ^a,b   Yuan, Ye ^a,b   Ge, Honghua ^a,b   Li, Kuai ^a,b   Zhao, Wei ^a,b   Gao, Yongxiang ^a,b   Niu, Liwen ^a,b   Teng, Maikun ^a,b  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

^b INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

Author keywords

Additional C terminus; Crystal structure; Homodimer; SGNH hydrolase; Substrate access

Indexed keywords

ESTERASE; ISOAMYLACETATE HYDROLYZING ESTERASE; MUTANT PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME STRUCTURE; GEL PERMEATION CHROMATOGRAPHY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; WILD TYPE;

AMINO ACID SEQUENCE; CARBOXYLIC ESTER HYDROLASES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ENZYME ASSAYS; MOLECULAR SEQUENCE DATA; PROTEIN MULTIMERIZATION; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY, PROTEIN;

SACCHAROMYCES CEREVISIAE;

EID: 78650791522     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22865     Document Type: Article

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